ACCD_DRIGR
ID ACCD_DRIGR Reviewed; 494 AA.
AC Q06GY8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01395};
DE Short=ACCase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01395};
GN Name=accD {ECO:0000255|HAMAP-Rule:MF_01395};
OS Drimys granadensis.
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Canellales; Winteraceae; Drimys.
OX NCBI_TaxID=224735;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17020608; DOI=10.1186/1471-2148-6-77;
RA Cai Z., Penaflor C., Kuehl J.V., Leebens-Mack J., Carlson J.E.,
RA dePamphilis C.W., Boore J.L., Jansen R.K.;
RT "Complete plastid genome sequences of Drimys, Liriodendron, and Piper:
RT implications for the phylogenetic relationships of magnoliids.";
RL BMC Evol. Biol. 6:77-77(2006).
CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its
CC carrier protein (BCCP) and then the CO(2) group is transferred by the
CC transcarboxylase to acetyl-CoA to form malonyl-CoA. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01395};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01395};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01395};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01395}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC carboxyl carrier protein, biotin carboxylase and 2 subunits each of
CC ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
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DR EMBL; DQ887676; ABH88306.1; -; Genomic_DNA.
DR RefSeq; YP_784395.1; NC_008456.1.
DR AlphaFoldDB; Q06GY8; -.
DR SMR; Q06GY8; -.
DR GeneID; 4363571; -.
DR UniPathway; UPA00655; UER00711.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011762; COA_CT_N.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR PRINTS; PR01070; ACCCTRFRASEB.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00515; accD; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Nucleotide-binding;
KW Plastid; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..494
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta, chloroplastic"
FT /id="PRO_0000359137"
FT DOMAIN 230..494
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT ZN_FING 234..256
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
SQ SEQUENCE 494 AA; 55528 MW; 4FA190C2FCC3A123 CRC64;
MEKWWFNSML SNEELEHRCG LSKSMNSLGR AIGNTSGSED LIINDTDKNI HSWSDSGSYS
CNNVDDLFGI RDIWSFVSDD TFLVRDSNGD SYSVYFDIEN QIFQIDNDSS FLSELESSFS
NYLNFSYLNS GSKSDNRYYD RYMYDIKYSW NNHINSCIDS YLHSEISIES YISSSSDNYG
DSYISSFICN ESVSVSDNGS SSIRTSGNGS DFNIRGRSND FDINQKYRHL WVQCENCYGL
NYKKFFRSKM NICEQCGYHL KMSSSDRIEL SIDPGTWDPM DEDMVSIDPI EFHSEEEPYR
DRIDSYQRKT GLTEAVQTGI GQLNGIPIAI GVMDFQFMGG SMGSVVGEKI TRLIEYATNG
SLPIIMVCAS GGARMQEGSL SLMQMAKISS ASYNYQSNKK LFYVSILTSP TTGGVTASFG
MLGDIIIAEP NAYIAFAGKR VIEQTLNKTV PDGSQAAEYS FHKGLFDSIV PRNPLKGVLS
ELFQLHGFFP LNQN
